It is an integrin complex containing INTEGRIN ALPHAIIB and INTEGRIN BETA3 which recognizes the arginine-glycine-aspartic acid (RGD) sequence present on several adhesive proteins. (harvard.edu)
Integrin beta3 occurs as three alternatively spliced isoforms, designated beta3A-C. (lookformedical.com)
Ligand binding to integrin alpha2beta1 triggers a cascade of intracellular signaling, including activation of p38 MAP kinase. (nih.gov)
Subunit2
An integrin beta subunit of approximately 85-kDa in size which has been found in INTEGRIN ALPHAIIB-containing and INTEGRIN ALPHAV-containing heterodimers. (lookformedical.com)
The CD49b protein is an integrin alpha subunit. (wikidoc.org)
Gene2
Subsequent screening for structural variants in candidate genes located in the same regions identified a homozygous deletion that includes exons 17 to 23 of the integrin beta 4 ( ITGB4 ), a gene that was previously associated with the same defect in humans. (biomedcentral.com)
Integrin alpha-2 or CD49b (cluster of differentiation 49b) is a protein which in humans is encoded by the CD49b gene . (wikidoc.org)
Triggers1
Moreover, PVRL4 triggers a form of signaling between the cells called integrin β4 signaling that allows them to survive without being anchored to the extracellular matrix. (elifesciences.org)
Progression1
β4-integrin/PI3K Signaling Promotes Tumor Progression through Galectin-3-N-glycan Complex. (fmu.ac.jp)
Beta1
Integrins are heterodimeric integral membrane glycoproteins composed of a distinct alpha chain and a common beta chain. (wikidoc.org)
Activation1
PVRL4 promotes anchorage-independence by driving cell-to-cell attachment and matrix-independent integrin β4/SHP-2/c-Src activation. (elifesciences.org)
Independent1
2003. Autocrine laminin-5 ligates alpha6beta4 integrin and activates RAC and NFkappaB to mediate anchorage-independent survival of mammary tumors. . (ucsf.edu)
Receptor3
Integrin α6β4 is an essential, dynamic adhesion receptor for laminin 332 found on epithelial cells, required for formation of strong cell-extracellular matrix (ECM) adhesion and induced migration, and coordinated by regions of the β4C cytoplasmic domain. (nih.gov)
La integrina alfa6beta4 también se encuentra en los timocitos, fibroblastos y células de Schwann, dónde funciona como receptor de laminina (RECEPTORES DE LAMININA) y está implicada en la cicatrización de heridas, la migración celular y la invasividad tumoral. (bvsalud.org)
Integrin alpha6beta4 is also found on thymocytes, fibroblasts, and Schwann cells, where it functions as a laminin receptor (RECEPTORS, LAMININ) and is involved in wound healing, cell migration, and tumor invasiveness. (bvsalud.org)
Beta4-integrin1
4. Keratinocytes display normal proliferation, survival and differentiation in conditional beta4-integrin knockout mice. (nih.gov)
5. Interaction of nectin-like molecule 2 with integrin alpha6beta4 and inhibition of disassembly of integrin alpha6beta4 from hemidesmosomes. (nih.gov)
14. The Tongue Squamous Carcinoma Cell Line Cal27 Primarily Employs Integrin α6β4-Containing Type II Hemidesmosomes for Adhesion Which Contribute to Anticancer Drug Sensitivity. (nih.gov)
As part of a complex network of proteins in hemidesmosomes, α6β4 integrin helps to hold the layers of skin together. (medlineplus.gov)
Laminin1
2003. Autocrine laminin-5 ligates alpha6beta4 integrin and activates RAC and NFkappaB to mediate anchorage-independent survival of mammary tumors. . (ucsf.edu)
Activates1
The integrin protein activates key signaling molecules, which trigger cancer cells to migrate through the body and invade other tissues. (medlineplus.gov)
Molecule1
An unusually small rotation between domains 9 and 10 creates a distinctive binding site, in which the RGD loop from domain 10 and the "synergy" region from domain 9 are on the same face of FN7-10 and thus easily accessible to a single integrin molecule. (embl.de)
Adhesion4
This conformational switch is correlated with the way alpha6beta4 promotes stable adhesion or cell migration and suggests an allosteric control of the integrin. (nih.gov)
Integrins are a group of proteins that regulate the attachment of cells to one another (cell-cell adhesion) and to the surrounding network of proteins and other molecules (cell-matrix adhesion). (medlineplus.gov)
Integrins are a family of heterodimeric glycoproteins involved in bidirectional cell signaling and participate in the regulation of cell shape, adhesion, migration, differentiation, gene transcription, survival and proliferation. (biomedcentral.com)
Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain that function in cell surface adhesion and signaling. (cancerindex.org)
The alpha 6 beta 4 integrin may promote tumorigenesis, while the alpha 6 beta 1 integrin may negatively regulate erbB2/HER2 signaling. (cancerindex.org)
Heterodimeric1
Integrins are a family of cell surface αβ heterodimeric transmembrane receptors for extracellular matrix components and cell-cell interactions. (biomedcentral.com)
Protein5
10. Protein kinase Cdelta-mediated phosphorylation of alpha6beta4 is associated with reduced integrin localization to the hemidesmosome and decreased keratinocyte attachment. (nih.gov)
The α6β4 integrin protein plays a particularly important role in strengthening and stabilizing the skin. (medlineplus.gov)
Mutations that lead to a complete or near-complete loss of α6β4 integrin tend to cause more severe signs and symptoms of EB-PA, while mutations that alter the structure or stability of this protein usually cause milder signs and symptoms. (medlineplus.gov)
The differences in protein and mRNA levels in cancer tissues and non-cancerous tissues were analyzed, and we subsequently investigated the association between integrin α6 expression and key parameters indicating lung adenocarcinoma progression and overall survival rate. (cancerindex.org)
Proteins1
The gene encodes a member of the integrin alpha chain family of proteins. (cancerindex.org)
Progression4
Researchers believe that α6β4 integrin may play a critical role in the progression of cancerous tumors called carcinomas. (medlineplus.gov)
Changes in the location and activity of α6β4 integrin within cancer cells are associated with the progression of carcinomas. (medlineplus.gov)
Recent studies suggest that, in addition to its role in the progression of existing carcinomas, α6β4 integrin may be involved in the initial formation of these tumors. (medlineplus.gov)
In this context it is not surprising to have identified integrin involvement in cancer progression. (biomedcentral.com)
Regulate cell1
Integrins also transmit chemical signals that regulate cell growth and the activity of certain genes. (medlineplus.gov)
Correlation2
Indeed, over-expression of the αvβ3, α5β1, αvβ5 and α6β4 integrins in various cancer types and correlation with the metastatic behaviour of breast, prostate and lung cancers as well as melanomas are well documented [ 4 ]. (biomedcentral.com)
To study integrin α6 expression in lung adenocarcinoma tissue through comparison with matching adjacent non-cancerous tissues as well as elucidating the correlation between integrin α6 expression with the clinical parameters of lung adenocarcinoma. (cancerindex.org)
Adenocarcinoma1
Elevated integrin α6 expression is involved in the occurrence and development of lung adenocarcinoma, and predicts a poor prognosis: a study based on immunohistochemical analysis and bioinformatics. (cancerindex.org)
Variant1
Integrin α6β4E variant is associated with actin and CD9 structures and modifies the biophysical properties of cell-cell and cell-extracellular matrix interactions. (nih.gov)
Expression1
Indeed, nothing is known about integrin α1β1 expression in CRC. (biomedcentral.com)
Alpha1
Alpha 6 beta 4 integrin abnormalities in junctional epidermolysis bullosa with pyloric atresia. (medlineplus.gov)
Cell1
9. Regulation of hemidesmosome dynamics and cell signaling by integrin α6β4. (nih.gov)
Complex1
We describe the crystal structure at 2.75 A resolution of the primary alpha6beta4-plectin complex, formed by the first pair of fibronectin type III domains and the N-terminal region of the connecting segment of beta4 and the actin-binding domain of plectin. (nih.gov)
Cells2
A shortage of functional α6β4 integrin causes cells in the epidermis to be fragile and easily damaged. (medlineplus.gov)
Activation of p53 function in carcinoma cells by the alpha6beta4 integrin. (uniroma1.it)